Some structural properties of recombinant HIV-1 protease

Nguyen Thi Hong Loan, Nguyen Van Sang, Trinh Hong Thai, Phan Tuan Nghia, Bui Phuong Thuan
Author affiliations


  • Nguyen Thi Hong Loan Trường Đại học Khoa học Tự nhiên, Đại học Quốc gia Hà Nội
  • Nguyen Van Sang
  • Trinh Hong Thai
  • Phan Tuan Nghia
  • Bui Phuong Thuan



3D structure, HIV-1, HIV-1 protease, primary structure, secondary structure


HIV-1PrHis Protease was produced in the recombinant form of 114 amino acid residues (ca. 12.8 kDa), consisting of 99 amino acid peptide of HIV-1 protease fused with TEV and 6xHis sequences at the C terminal. The MS/MS analysis indicated that the amino acid sequence of HIV-1PrHis was exactly the same as theoretically designed. The circular dichroism spectrum of the HIV-1PrHis showed clear β sheet with a negative peak at 205 nm and intensity of nearly -8 mdeg. By using ProMod-II software and based on 3D structures of reported HIV-1 proteases, 3D structure of the HIV-1PrHis was deduced, it had RMSD of 0.154 Å; TM-score of 0.9882 and Z-core in the same range of the known HIV-1proteases analyzed by NMR and X-ray diffraction. The obtained results will enable to use the recombinant HIV-1PrHis for screening its inhibitors.


Download data is not yet available.


Metrics Loading ...




How to Cite

Hong Loan, N. T., Sang, N. V., Thai, T. H., Nghia, P. T., & Thuan, B. P. (2016). Some structural properties of recombinant HIV-1 protease. Academia Journal of Biology, 37(4), 520–527.




Most read articles by the same author(s)

1 2 > >>